The disulfide bridge pattern of snake venom disintegrins, flavoridin and echistatin

FEBS Letters

Mann, Karlheinz²  Schäfer, Wolfram²  Stewart, Gwendolyn J.¹  Wang, Yuqin¹  Calvete, Juan J.²  Niewiarowski, Stefan¹ 

[1] Department of Physiology and Sol Sherry Trombosis Research Centers, Temple University School of Medicine, Philadelphia, PA 19140, USA;Max-Planck-Institut für Biochemie, W-8033 Martinsried, Germany

关键词: Inhibitor of integrin: Disintegrin;    Disullfide bridge;    Echistatin;    Flavoridin;   

DOI  :  10.1016/0014-5793(92)80797-K

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Flavoridin and echistatin, isolated from the venom of Trimeresurus flavoviridis and Echis carinatus, respectively, belong to the disintegrin family of integrin β₁ and β₃ inhibitors of low molecular weight RGD-containing, cysteine-rich peptides. Since disulfide bonds are critical for expression of biological activity, we sought to determine their location in these two proteins. In flavoridin, direct evidence for the existence of linkage between Cys⁴-Cys¹⁰ and between Cys⁴⁵ and Cys⁶⁴ was obtained by analysis of proteolytic products, and indirect evidence suggests links between Cys¹³-Cys¹⁴ and Cys¹³-Cys¹⁴. In echistatin, links between Cys¹⁴-Cys³⁷ and Cys²⁰-Cys³⁴ were identified by direct chemical analysis.

【 授权许可】

Unknown